PMID: 8593103Feb 1, 1996Paper

Primary structure and properties of the formyltransferase from the mesophilic Methanosarcina barkeri: comparison with the enzymes from thermophilic and hyperthermophilic methanogens

Archives of Microbiology
J KunowR K Thauer

Abstract

The ftr gene encoding formylmethanofuran: tetrahydromethanopterin formyltransferase (Ftr) from Methanosarcina barkeri was cloned, sequenced, and functionally expressed in Escherichia coli. The overproduced enzyme was purified eightfold to apparent homogeneity, and its catalytic properties were determined. The primary structure and the hydropathic character of the formyltransferase from Methanosarcina barkeri were compared with those of the enzymes from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri. The amino acid sequence of the enzyme from Methanosarcina barkeri was 64%, 61%, and 59% identical to that of the enzyme from Methanobacterium thermoautotrophicum, Methanothermus fervidus, and Methanopyrus kandleri, respectively. A negative correlation between the hydrophobicity of the enzymes and both the growth temperature optimum and the intracellular salt concentration of the four organisms was observed. The hydrophobicity of amino acid composition was +21.6 for the enzyme from Methanosarcina barkeri (growth temperature optimum 37 degrees C, intracellular salt concentrationapproximately 0.3 M), +9.9 for the enzyme from Methanobacterium thermoautotrophicum (65 degrees C,approximately 0.7 M...Continue Reading

Citations

Oct 20, 2005·Journal of Bioscience and Bioengineering·Seigo ShimaUlrich Ermler
Sep 5, 2001·European Journal of Biochemistry·B K Pomper, J A Vorholt
Dec 1, 1998·Journal of Applied Microbiology·M W Adams
Feb 10, 2006·Journal of Molecular Biology·Priyamvada AcharyaSeigo Shima
Sep 20, 2019·Microbiology and Molecular Biology Reviews : MMBR·Thomas D Mand, William W Metcalf
Mar 17, 1999·FEMS Microbiology Reviews·J G Ferry
Oct 27, 1997·Journal of Bacteriology·J N ReeveD R Smith

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